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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 4 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.1 Publication

Catalytic activityi

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

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi600Zinc1
Metal bindingi604Zinc1
Metal bindingi703Zinc1
Metal bindingi707Zinc1

GO - Molecular functioni

  • alanine-tRNA ligase activity Source: UniProtKB-HAMAP
  • aminoacyl-tRNA editing activity Source: UniProtKB
  • ATP binding Source: UniProtKB-HAMAP
  • tRNA binding Source: UniProtKB-KW
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • alanyl-tRNA aminoacylation Source: UniProtKB
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. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Gene namesi
Name:alaS
Ordered Locus Names:AF_2255
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi703C → A: Loss of tRNA editing activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000752601 – 906Alanine--tRNA ligaseAdd BLAST906

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-48856N.
STRINGi224325.AF2255.

Structurei

Secondary structure

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 7Combined sources5
Helixi11 – 14Combined sources4
Turni15 – 17Combined sources3
Beta strandi19 – 21Combined sources3
Beta strandi25 – 28Combined sources4
Beta strandi30 – 32Combined sources3
Beta strandi35 – 38Combined sources4
Beta strandi42 – 45Combined sources4
Beta strandi55 – 58Combined sources4
Helixi62 – 74Combined sources13
Turni75 – 77Combined sources3
Beta strandi92 – 96Combined sources5
Helixi100 – 104Combined sources5
Turni105 – 110Combined sources6
Beta strandi111 – 113Combined sources3
Beta strandi116 – 127Combined sources12
Helixi129 – 134Combined sources6
Turni135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi143 – 155Combined sources13
Helixi163 – 176Combined sources14
Helixi181 – 183Combined sources3
Beta strandi185 – 193Combined sources9
Beta strandi196 – 205Combined sources10
Beta strandi208 – 220Combined sources13
Beta strandi226 – 228Combined sources3
Beta strandi231 – 246Combined sources16
Helixi247 – 255Combined sources9
Helixi260 – 264Combined sources5
Helixi266 – 274Combined sources9
Beta strandi282 – 284Combined sources3
Helixi285 – 301Combined sources17
Helixi307 – 320Combined sources14
Helixi324 – 352Combined sources29
Helixi361 – 379Combined sources19
Helixi386 – 397Combined sources12
Helixi405 – 437Combined sources33
Helixi442 – 452Combined sources11
Helixi456 – 465Combined sources10
Helixi476 – 482Combined sources7
Turni508 – 510Combined sources3
Beta strandi516 – 525Combined sources10
Beta strandi528 – 534Combined sources7
Beta strandi548 – 552Combined sources5
Beta strandi555 – 559Combined sources5
Beta strandi561 – 565Combined sources5
Beta strandi568 – 572Combined sources5
Beta strandi583 – 588Combined sources6
Helixi590 – 614Combined sources25
Beta strandi620 – 622Combined sources3
Beta strandi631 – 635Combined sources5
Helixi642 – 657Combined sources16
Beta strandi661 – 668Combined sources8
Helixi669 – 676Combined sources8
Helixi678 – 681Combined sources4
Beta strandi688 – 696Combined sources9
Beta strandi699 – 702Combined sources4
Helixi711 – 714Combined sources4
Beta strandi717 – 726Combined sources10
Beta strandi729 – 737Combined sources9
Helixi738 – 740Combined sources3
Helixi742 – 756Combined sources15
Turni757 – 759Combined sources3
Helixi762 – 764Combined sources3
Helixi765 – 799Combined sources35
Beta strandi803 – 807Combined sources5
Beta strandi809 – 814Combined sources6
Helixi819 – 831Combined sources13
Beta strandi834 – 841Combined sources8
Beta strandi843 – 856Combined sources14
Helixi858 – 869Combined sources12
Beta strandi871 – 875Combined sources5
Beta strandi877 – 886Combined sources10
Helixi890 – 904Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZTGX-ray2.20A1-739[»]
2ZVFX-ray3.20A/B/C/D/E/F/G/H737-906[»]
3WQYX-ray3.30A/B1-906[»]
3WQZX-ray3.49A/B1-906[»]
ProteinModelPortaliO28029.
SMRiO28029.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO28029.

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01255. Archaea.
COG0013. LUCA.
KOiK01872.
OMAiLDVTHYK.

Family and domain databases

HAMAPiMF_00036_A. Ala_tRNA_synth_A. 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.
IPR022429. Ala-tRNA_lgiase_arc.
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.
TIGRFAMsiTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O28029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLDEEYLDI TFLTENGFVR KRCPKCGKHF WTADPEREIC GDPPCESYSF
60 70 80 90 100
IGNPVFKKPF ELDEMREYYL NFFERRGHGR IERYPVVARW RTDIYLTIAS
110 120 130 140 150
IADFQPFVTS GVAPPPANPL TISQPCIRLD DLDSVGRTGR HLTLFEMMAH
160 170 180 190 200
HAFNYPGKEI YWKNETVAYC TELLNELGVK KEDIVYKEEP WAGGGNAGPC
210 220 230 240 250
LEAIVGGLEV ATLVFMNLEE HPEGDIEIKG ARYRKMDNYI VDTGYGLERF
260 270 280 290 300
VWASKGTPTV YDAIFPEVVD TIIDNSNVSF NREDERVRRI VAESSKLAGI
310 320 330 340 350
MGELRGERLN QLRKSVADTV GVSVEELEGI VVPLEKVYSL ADHTRCILFM
360 370 380 390 400
LGDGLVPSNA GAGYLARLMI RRSLRLAEEL ELGLDLYDLV EMHKKILGFE
410 420 430 440 450
FDVPLSTVQE ILELEKERYR TTVSKGTRLV ERLVERKKKL EKDDLIELYD
460 470 480 490 500
SHGIPVELAV GIAAEKGAEV EMPKDIYAEL AKRHSKAEKV QEKKITLQNE
510 520 530 540 550
YPATEKLYYD DPTLLEFEAE VIGVEGDFVI LNRSAFYPES GGQDNDVGYL
560 570 580 590 600
IANGGKFEVV DVLEADGVVL HVVKGAKPEV GTKVKGVIDS DVRWRHMRHH
610 620 630 640 650
SATHVLLYSL QKVLGNHVWQ AGARKEFSKA RLDVTHFRRP SEEEIKEIEM
660 670 680 690 700
LANREILANK PIKWEWMDRI EAERKFGFRL YQGGVPPGRK IRVVQVGDDV
710 720 730 740 750
QACGGTHCRS TGEIGMLKIL KVESIQDGVI RFEFAAGEAA IEAVEEMERL
760 770 780 790 800
LREASSILRV EPAKLPKTVE RFFEEWKDQR KEIERLKSVI ADLWADILME
810 820 830 840 850
RAEEFDSMKV VAEVVDADMQ ALQKLAERLA EKGAVGCLMA KGEGKVFVVT
860 870 880 890 900
FSGQKYDARE LLREIGRVAK GSGGGRKDVA QGAVQQLLDR EEMLDVIFRF

LSEHEG
Length:906
Mass (Da):102,536
Last modified:January 1, 1998 - v1
Checksum:i2AD39B7B65C72C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89002.1.
PIRiG69531.
RefSeqiWP_010879744.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89002; AAB89002; AF_2255.
GeneIDi24796018.
KEGGiafu:AF_2255.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89002.1.
PIRiG69531.
RefSeqiWP_010879744.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZTGX-ray2.20A1-739[»]
2ZVFX-ray3.20A/B/C/D/E/F/G/H737-906[»]
3WQYX-ray3.30A/B1-906[»]
3WQZX-ray3.49A/B1-906[»]
ProteinModelPortaliO28029.
SMRiO28029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48856N.
STRINGi224325.AF2255.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89002; AAB89002; AF_2255.
GeneIDi24796018.
KEGGiafu:AF_2255.

Phylogenomic databases

eggNOGiarCOG01255. Archaea.
COG0013. LUCA.
KOiK01872.
OMAiLDVTHYK.

Enzyme and pathway databases

BRENDAi6.1.1.7. 414.

Miscellaneous databases

EvolutionaryTraceiO28029.

Family and domain databases

HAMAPiMF_00036_A. Ala_tRNA_synth_A. 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.
IPR022429. Ala-tRNA_lgiase_arc.
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.
TIGRFAMsiTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYA_ARCFU
AccessioniPrimary (citable) accession number: O28029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 112 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.