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O83980 (SYA_TREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase
EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:TP_1017
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Treponema ›

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00036_B

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036_B

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

Consists of two domains; the N-terminal catalytic domain (in this organism this is shorter than usual) and the editing domain; the C-terminal C-Ala domain found in most orthologs is missing. The editing domain removes incorrectly charged amino acids By similarity. HAMAP-Rule MF_00036_B

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Alanine--tRNA ligase HAMAP-Rule MF_00036_B
PRO_0000075237

Sites

Metal binding4631Zinc Potential
Metal binding4671Zinc Potential
Metal binding5651Zinc Potential
Metal binding5691Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
O83980 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 9EB42BC1C86DF4C4

FASTA60567,187
        10         20         30         40         50         60 
MSIPIRADQL RSRYLAFFSQ KAHVVISGKS LVPEHDPTVL FTTAGMHPLV PYLMGEPHPA 

        70         80         90        100        110        120 
GTRLVNAQKC LRTGDIDAVG DNSHLTFFEM LGNWSLGDYF KEEAIAFSFE FLTGAPWLGI 

       130        140        150        160        170        180 
SPDRLSVTVF AGDEAVARDE ESAAIWERLG IARTHIHFLP RADNWWGPTG ETGPCGPDTE 

       190        200        210        220        230        240 
IFFDTGVPPC SVSCRPGCSC GKYVEIWNDV FMQYRKDADG RYRPLERYCV DTGMGIERTV 

       250        260        270        280        290        300 
AVLQGKRSVY DTEIFTPLLE RIGQLCGKRY GCQGAHDVSM RIVCDHIRAA TFILGDPVPV 

       310        320        330        340        350        360 
RPSNVGAGYV LRRIIRRSVR HGRKLGIDGE FLSSLARVVI GQYAAVYPEL EEKATCIAQE 

       370        380        390        400        410        420 
LANEERKFLD ALRKGEAEYE RMIPKFLQGT EREIPGSVAF RLYDTYGFPL ELTEELARES 

       430        440        450        460        470        480 
GLRVDRAGFD TAFQAHQACS RIGAQRVFKG GLADHSAETT AYHTATHLLH QALRVVLGTH 

       490        500        510        520        530        540 
VQQKGSNITA ERLRFDFSHP RPMSAQEKVQ VEQLVNEQIR ADLPVCCEVM SLEDAMNSGA 

       550        560        570        580        590        600 
VALFGEKYES TVKVYSIGTF SREVCGGPHV ARTGQLGRFS IQKEQSSAAG VRRIRAILEK 


SGEKS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000520 Genomic DNA. Translation: AAC65968.1.
PIRE71253.
RefSeqNP_219454.1. NC_000919.1.

3D structure databases

ProteinModelPortalO83980.
ModBaseSearch...

Protein-protein interaction databases

IntActO83980. 1 interaction.
STRING243276.TP1017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC65968; AAC65968; TP_1017.
GeneID2610864.
KEGGtpa:TP1017.
PATRIC20532159. VBITrePal57110_1072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
KOK01872.
OMASFEFLTS.
ProtClustDBPRK01584.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B. Divergent sequence.
InterProIPR002318. 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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_TREPA
AccessionPrimary (citable) accession number: O83980
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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