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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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). Edits incorrectly charged Ser-tRNA(Ala). Incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Gly and Ser) in the charging step.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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi613 – 6131Zinc
Metal bindingi617 – 6171Zinc
Metal bindingi717 – 7171Zinc

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

BioCyciPHOR70601:GJWR-281-MONOMER.
BRENDAi6.1.1.7. 5244.

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:PH0297
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi633 – 6331Q → M: Significant deacylation of correctly charged L-alanyl-tRNA(Ala) occurs. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 915915Alanine--tRNA ligasePRO_0000075274Add
BLAST

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi70601.PH0297.

Structurei

Secondary structure

1
915
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 125Combined sources
Beta strandi16 – 194Combined sources
Turni21 – 233Combined sources
Beta strandi26 – 305Combined sources
Turni40 – 423Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 554Combined sources
Helixi59 – 7113Combined sources
Beta strandi74 – 763Combined sources
Helixi100 – 1045Combined sources
Turni105 – 1117Combined sources
Beta strandi116 – 12712Combined sources
Helixi132 – 1343Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 15412Combined sources
Helixi163 – 17614Combined sources
Helixi182 – 1843Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi209 – 22113Combined sources
Beta strandi231 – 2333Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 25216Combined sources
Helixi253 – 2619Combined sources
Helixi266 – 2705Combined sources
Helixi272 – 28211Combined sources
Helixi289 – 30012Combined sources
Beta strandi304 – 3085Combined sources
Helixi310 – 32112Combined sources
Helixi325 – 35329Combined sources
Beta strandi359 – 3613Combined sources
Helixi362 – 38019Combined sources
Helixi387 – 39812Combined sources
Turni399 – 4013Combined sources
Helixi404 – 4074Combined sources
Helixi409 – 44436Combined sources
Helixi451 – 46111Combined sources
Helixi465 – 4728Combined sources
Turni474 – 4763Combined sources
Helixi485 – 4906Combined sources
Helixi491 – 4944Combined sources
Beta strandi507 – 5137Combined sources
Helixi519 – 5224Combined sources
Beta strandi528 – 53710Combined sources
Beta strandi540 – 5467Combined sources
Beta strandi560 – 5645Combined sources
Beta strandi567 – 57711Combined sources
Beta strandi580 – 5867Combined sources
Helixi588 – 5903Combined sources
Beta strandi596 – 6016Combined sources
Helixi603 – 62725Combined sources
Beta strandi632 – 6387Combined sources
Beta strandi643 – 6486Combined sources
Helixi655 – 67117Combined sources
Beta strandi674 – 6818Combined sources
Helixi682 – 6898Combined sources
Helixi691 – 6933Combined sources
Beta strandi695 – 6973Combined sources
Beta strandi701 – 7099Combined sources
Turni710 – 7123Combined sources
Beta strandi713 – 7164Combined sources
Helixi725 – 7284Combined sources
Beta strandi731 – 74010Combined sources
Beta strandi743 – 7508Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZZEX-ray2.16A/B1-752[»]
2ZZFX-ray2.70A1-752[»]
2ZZGX-ray3.10A/B1-752[»]
ProteinModelPortaliO58035.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58035.

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 (By similarity).By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01255. Archaea.
COG0013. LUCA.
HOGENOMiHOG000015496.
KOiK01872.
OMAiLDVTHYK.

Family and domain databases

HAMAPiMF_00036_A. Ala_tRNA_synth_A.
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.

O58035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFIMKTRMF EEEGWIRKKC KVCGKPFWTL DPDRETCGDP PCDEYQFIGK
60 70 80 90 100
PGIPRKYTLD EMREKFLRFF EKHEIYPHGR VKRYPVLPRW RDDVLLVGAS
110 120 130 140 150
IMDFQPWVIS GEADPPANPL VISQPSIRFT DIDNVGITGR HFTIFEMMAH
160 170 180 190 200
HAFNYPGKPI YWMDETVELA FEFFTKELKM KPEDITFKEN PWAGGGNAGP
210 220 230 240 250
AFEVLYRGLE VATLVFMQYK KAPENAPQDQ VVVIKGEKYI PMETKVVDTG
260 270 280 290 300
YGLERLVWMS QGTPTAYDAV LGYVVEPLKK MAGIEKIDEK ILMENSRLAG
310 320 330 340 350
MFDIEDLGDL RYLREQVAKR VGITVEELEK AIRPYELIYA IADHTKALTF
360 370 380 390 400
MLADGVVPSN VKAGYLARLL IRKSIRHLRE LGLEVPLSEI VALHIKELHK
410 420 430 440 450
TFPEFKEMED IILEMIELEE KKYAETLRRG SDLVRREIAK LKKKGIKEIP
460 470 480 490 500
VEKLVTFYES HGLTPEIVKE IAEKEGVKVN IPDNFYSMVA KEAERTKEEK
510 520 530 540 550
GEELVDFELL KDLPDTRRLY YEDPFMKEFD AKVLRVIKDW VILDATAFYP
560 570 580 590 600
EGGGQPYDTG VLIVNGREVK VTNVQKVGKV IIHKVEDPGA FKEGMIVHGK
610 620 630 640 650
IDWKRRIQHM RHHTGTHVLM GALVRVLGRH VWQAGSQLTT DWARLDISHY
660 670 680 690 700
KRISEEELKE IEMLANRIVM EDRKVTWEWL PRTTAEQKYG FRLYQGGVVP
710 720 730 740 750
GREIRVVKIE DWDVQACGGT HLPSTGLVGP IKILRTERIQ DGVERIIFAC
760 770 780 790 800
GEAAIREWQK ERDLLKKASN VLRVPPEKLP ETAERFFNEW KEARKEVDKL
810 820 830 840 850
KKELARLLVY ELESKMQKIG SIEFIGEVVE GSMEDLRELV EKLKKPKRVV
860 870 880 890 900
VLISRDGYFA VSVGSEVGVE ANELAKKITL IAGGGGGGRR DIAQGKVKDI
910
SKAKDVIESI KSMFS
Length:915
Mass (Da):105,011
Last modified:August 1, 1998 - v1
Checksum:iAFD4C26939928D33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29370.1.
PIRiC71455.
RefSeqiWP_010884393.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29370; BAA29370; BAA29370.
GeneIDi1444180.
KEGGipho:PH0297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29370.1.
PIRiC71455.
RefSeqiWP_010884393.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZZEX-ray2.16A/B1-752[»]
2ZZFX-ray2.70A1-752[»]
2ZZGX-ray3.10A/B1-752[»]
ProteinModelPortaliO58035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29370; BAA29370; BAA29370.
GeneIDi1444180.
KEGGipho:PH0297.

Phylogenomic databases

eggNOGiarCOG01255. Archaea.
COG0013. LUCA.
HOGENOMiHOG000015496.
KOiK01872.
OMAiLDVTHYK.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-281-MONOMER.
BRENDAi6.1.1.7. 5244.

Miscellaneous databases

EvolutionaryTraceiO58035.

Family and domain databases

HAMAPiMF_00036_A. Ala_tRNA_synth_A.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. Cited for: FUNCTION, MUTAGENESIS OF GLN-633.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 1-752 IN THE PRESENCE AND ABSENCE OF AN ALANYL-ADENYLATE ANALOG, ZINC-BINDING, COFACTOR.

Entry informationi

Entry nameiSYA_PYRHO
AccessioniPrimary (citable) accession number: O58035
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Unlike the case in Archaeoglobus fulgidus and some of the free-standing tRNA(Ala) AlaX editing proteins, His-721 does not bind zinc but forms a hydrogen bond with Cys-717 instead.Curated

Keywords - Technical termi

3D-structure, Complete 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.