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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)DescriptionActionsGraphical viewLength
Metal bindingi559ZincUniRule annotation1
Metal bindingi563ZincUniRule annotation1
Metal bindingi661ZincUniRule annotation1
Metal bindingi665ZincUniRule annotation1

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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000750471 – 867Alanine--tRNA ligaseAdd BLAST867

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_1293.

Structurei

Secondary structure

1867
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 17Combined sources13
Turni18 – 20Combined sources3
Beta strandi22 – 24Combined sources3
Helixi45 – 47Combined sources3
Helixi48 – 51Combined sources4
Beta strandi60 – 69Combined sources10
Helixi78 – 80Combined sources3
Turni81 – 83Combined sources3
Beta strandi84 – 86Combined sources3
Beta strandi89 – 101Combined sources13
Helixi104 – 117Combined sources14
Helixi123 – 125Combined sources3
Beta strandi126 – 131Combined sources6
Helixi135 – 142Combined sources8
Turni143 – 145Combined sources3
Helixi149 – 151Combined sources3
Beta strandi152 – 155Combined sources4
Helixi157 – 160Combined sources4
Beta strandi161 – 179Combined sources19
Beta strandi182 – 184Combined sources3
Helixi186 – 189Combined sources4
Beta strandi190 – 203Combined sources14
Beta strandi205 – 207Combined sources3
Beta strandi209 – 222Combined sources14
Helixi223 – 230Combined sources8
Helixi236 – 238Combined sources3
Turni240 – 242Combined sources3
Helixi243 – 253Combined sources11
Beta strandi257 – 259Combined sources3
Helixi261 – 282Combined sources22
Helixi291 – 309Combined sources19
Helixi317 – 328Combined sources12
Turni329 – 331Combined sources3
Helixi334 – 373Combined sources40
Beta strandi377 – 379Combined sources3
Helixi381 – 389Combined sources9
Helixi395 – 403Combined sources9
Turni404 – 406Combined sources3
Helixi411 – 423Combined sources13
Turni424 – 426Combined sources3
Beta strandi443 – 445Combined sources3
Helixi446 – 449Combined sources4
Turni450 – 452Combined sources3
Beta strandi758 – 762Combined sources5
Beta strandi765 – 774Combined sources10
Helixi777 – 787Combined sources11
Beta strandi790 – 802Combined sources13
Beta strandi805 – 812Combined sources8
Helixi814 – 816Combined sources3
Turni817 – 819Combined sources3
Helixi822 – 832Combined sources11
Beta strandi841 – 849Combined sources9
Helixi851 – 853Combined sources3
Helixi854 – 866Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OrthoDBiPOG091H01PM.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B. 1 hit.
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
PDB 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.
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.
OrthoDBiPOG091H01PM.

Enzyme and pathway databases

BRENDAi6.1.1.7. 396.

Miscellaneous databases

EvolutionaryTraceiO67323.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B. 1 hit.
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...

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: November 2, 2016
This is version 109 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.