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Entry version 195 (07 Oct 2020)
Sequence version 2 (01 Nov 1997)
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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the attachment of L-alanine to tRNA(Ala) in a two-step reaction: L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser (PubMed:28362257). These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step.1 Publication
Edits mischarged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr) (PubMed:12554667, PubMed:18723508). Dtd edits Gly-tRNA(Ala) 4-fold better than does AlaRS (PubMed:28362257).3 Publications
Attaches Ala to transfer-messenger RNA (tmRNA, also known as 10Sa RNA, the product of the ssrA gene). tmRNA plays a major role in rescue of stalled ribosomes via trans-translation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 1 zinc ion per subunit; it is not clear where this binding occurs.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi564ZincBy similarity1
Metal bindingi568ZincBy similarity1
Metal bindingi666ZincBy similarity1
Metal bindingi670ZincBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, RNA-binding, tRNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ALAS-MONOMER
MetaCyc:ALAS-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.1.1.7, 2026

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P00957

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alanine--tRNA ligase (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:alaS
Synonyms:lovB
Ordered Locus Names:b2697, JW2667
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi179C → S: Inactivates the enzyme. 1 Publication1
Mutagenesisi182C → S: No inactivation. 1 Publication1
Mutagenesisi184E → Q: No inactivation. 1 Publication1
Mutagenesisi188D → N: No inactivation. 1 Publication1
Mutagenesisi189H → Q: Inactivates the enzyme. 1 Publication1
Mutagenesisi191D → N: No inactivation. 1 Publication1
Mutagenesisi192H → Q: Inactivates the enzyme. 1 Publication1
Mutagenesisi236D → A or N: Decreases affinity for alanine without improving discrimination against serine. 1 Publication1
Mutagenesisi238G → A: Greatly decreases affinity for alanine with only small changes in affinity for serine and glycine, in a 2-442 residue construct. 1 Publication1
Mutagenesisi564H → A: No effect on tRNA editing. 1 Publication1
Mutagenesisi567T → F: Complete loss of tRNA editing; when associated with W-587 and F-666. 1 Publication1
Mutagenesisi568H → A: No effect on tRNA editing. 1 Publication1
Mutagenesisi584Q → H: Loss of mischarged tRNA editing activity; when associated with A-666. 2 Publications1
Mutagenesisi587S → W: Complete loss of tRNA editing; when associated with F-567 and F-666. 1 Publication1
Mutagenesisi666C → A: Loss of mischarged tRNA editing activity; when associated with H-584 the effect is more pronounced. 3 Publications1
Mutagenesisi666C → F: Complete loss of tRNA editing; when associated with F-567 and W-587. 1 Publication1
Mutagenesisi670H → A: No effect on tRNA editing. 1 Publication1
Mutagenesisi693R → K: Reduces specificity of editing activity for tRNA(Ala), allows editing of tRNA(Thr). 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000751132 – 876Alanine--tRNA ligaseAdd BLAST875

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei74N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00957

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00957

PRoteomics IDEntifications database

More...
PRIDEi
P00957

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P00957

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00957

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P00957
With#Exp.IntAct
itself2EBI-544061,EBI-544061

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261283, 55 interactors
851507, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-9080N

Protein interaction database and analysis system

More...
IntActi
P00957, 21 interactors

STRING: functional protein association networks

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STRINGi
511145.b2697

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1876
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00957

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00957

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 461CatalyticAdd BLAST460
Regioni553 – 705EditingAdd BLAST153
Regioni699 – 808Important for oligomerizationAdd BLAST110
Regioni766 – 875C-Ala domainAdd BLAST110

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 editing domain removes incorrectly charged amino acids, i.e. Ser-tRNA(Ala) or Gly-tRNA(Ala) become uncharged tRNA(Ala) and the amino acid. It is specific for the acceptor stem of tRNA(Ala).
The C-terminal 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. This C-Ala domain can be replaced in vitro by the corresponding domain of Aquifex aeolicus or man. Recognition of tRNA(Ala) by the 2 domains is independent, that is one enzyme recognizes the same tRNA(Ala) in 2 different manners.Curated

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0013, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004485_1_1_6

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00957

KEGG Orthology (KO)

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KOi
K01872

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00957

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00036_B, Ala_tRNA_synth_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002318, 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_sf
IPR012947, tRNA_SAD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02272, DHHA1, 1 hit
PF01411, tRNA-synt_2c, 1 hit
PF07973, tRNA_SAD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00980, TRNASYNTHALA

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00863, tRNA_SAD, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF101353, SSF101353, 1 hit
SSF50447, SSF50447, 1 hit
SSF55186, SSF55186, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00344, alaS, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50860, AA_TRNA_LIGASE_II_ALA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P00957-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV
60 70 80 90 100
FLGLDKRNYS RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG
110 120 130 140 150
DYFKHDAIQF AWELLTSEKW FALPKERLWV TVYESDDEAY EIWEKEVGIP
160 170 180 190 200
RERIIRIGDN KGAPYASDNF WQMGDTGPCG PCTEIFYDHG DHIWGGPPGS
210 220 230 240 250
PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG LERIAAVLQH
260 270 280 290 300
VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM
310 320 330 340 350
PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK
360 370 380 390 400
RQQAQVEQVL KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD
410 420 430 440 450
TYGFPVDLTA DVCRERNIKV DEAGFEAAME EQRRRAREAS GFGADYNAMI
460 470 480 490 500
RVDSASEFKG YDHLELNGKV TALFVDGKAV DAINAGQEAV VVLDQTPFYA
510 520 530 540 550
ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG SLKVGDAVQA
560 570 580 590 600
DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH
610 620 630 640 650
NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD
660 670 680 690 700
ERVRVLSMGD FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG
710 720 730 740 750
EGAIATVHAD SDRLSEVAHL LKGDSNNLAD KVRSVLERTR QLEKELQQLK
760 770 780 790 800
EQAAAQESAN LSSKAIDVNG VKLLVSELSG VEPKMLRTMV DDLKNQLGST
810 820 830 840 850
IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG GKGGGRPDMA
860 870
QAGGTDAAAL PAALASVKGW VSAKLQ
Length:876
Mass (Da):96,032
Last modified:November 1, 1997 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i73F69C69FCF8C08C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti29 – 33LVPHN → RYPIT no nucleotide entry (PubMed:7005898).Curated5
Sequence conflicti29 – 33LVPHN → RYPIT in AAA03208 (PubMed:7025207).Curated5
Sequence conflicti158G → N no nucleotide entry (PubMed:7005898).Curated1
Sequence conflicti158G → N in AAA03208 (PubMed:7025207).Curated1
Sequence conflicti168D → G in AAA03208 (PubMed:7025207).Curated1
Sequence conflicti172Q → R in AAA03208 (PubMed:7025207).Curated1
Sequence conflicti175D → G in AAA03208 (PubMed:7025207).Curated1
Sequence conflicti180G → D in AAA03208 (PubMed:7025207).Curated1
Sequence conflicti584Q → H in AAA03208 (PubMed:7025207).Curated1
Sequence conflicti619Q → L in AAA03208 (PubMed:7025207).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75739.1
AP009048 Genomic DNA Translation: BAA16559.1
J01581 Unassigned DNA Translation: AAA03208.1
L07596 Unassigned DNA Translation: AAA71918.1 Sequence problems.
D44453 Genomic DNA Translation: BAA21554.1
Z28405 Genomic DNA Translation: CAA82247.1

Protein sequence database of the Protein Information Resource

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PIRi
E65049, SYECAT

NCBI Reference Sequences

More...
RefSeqi
NP_417177.1, NC_000913.3
WP_000047184.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75739; AAC75739; b2697
BAA16559; BAA16559; BAA16559

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947175

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2667
eco:b2697

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4046

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75739.1
AP009048 Genomic DNA Translation: BAA16559.1
J01581 Unassigned DNA Translation: AAA03208.1
L07596 Unassigned DNA Translation: AAA71918.1 Sequence problems.
D44453 Genomic DNA Translation: BAA21554.1
Z28405 Genomic DNA Translation: CAA82247.1
PIRiE65049, SYECAT
RefSeqiNP_417177.1, NC_000913.3
WP_000047184.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HXUX-ray2.10A2-442[»]
3HXVX-ray1.93A2-442[»]
3HXWX-ray1.93A2-442[»]
3HXXX-ray2.11A2-442[»]
3HXYX-ray2.27A2-442[»]
3HXZX-ray1.99A/B/C/D2-442[»]
3HY0X-ray1.90A/B2-442[»]
3HY1X-ray2.79A/B2-442[»]
SMRiP00957
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261283, 55 interactors
851507, 1 interactor
DIPiDIP-9080N
IntActiP00957, 21 interactors
STRINGi511145.b2697

Protein family/group databases

MoonProtiP00957

PTM databases

iPTMnetiP00957

2D gel databases

SWISS-2DPAGEiP00957

Proteomic databases

jPOSTiP00957
PaxDbiP00957
PRIDEiP00957

Genome annotation databases

EnsemblBacteriaiAAC75739; AAC75739; b2697
BAA16559; BAA16559; BAA16559
GeneIDi947175
KEGGiecj:JW2667
eco:b2697
PATRICifig|1411691.4.peg.4046

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB0033

Phylogenomic databases

eggNOGiCOG0013, Bacteria
HOGENOMiCLU_004485_1_1_6
InParanoidiP00957
KOiK01872
PhylomeDBiP00957

Enzyme and pathway databases

BioCyciEcoCyc:ALAS-MONOMER
MetaCyc:ALAS-MONOMER
BRENDAi6.1.1.7, 2026

Miscellaneous databases

EvolutionaryTraceiP00957

Protein Ontology

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PROi
PR:P00957

Family and domain databases

HAMAPiMF_00036_B, Ala_tRNA_synth_B, 1 hit
InterProiView protein in InterPro
IPR002318, 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_sf
IPR012947, tRNA_SAD
PfamiView protein in Pfam
PF02272, DHHA1, 1 hit
PF01411, tRNA-synt_2c, 1 hit
PF07973, tRNA_SAD, 1 hit
PRINTSiPR00980, TRNASYNTHALA
SMARTiView protein in SMART
SM00863, tRNA_SAD, 1 hit
SUPFAMiSSF101353, SSF101353, 1 hit
SSF50447, SSF50447, 1 hit
SSF55186, SSF55186, 1 hit
TIGRFAMsiTIGR00344, alaS, 1 hit
PROSITEiView protein in PROSITE
PS50860, AA_TRNA_LIGASE_II_ALA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00957
Secondary accession number(s): P78279
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: October 7, 2020
This is version 195 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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