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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 bindingi561ZincUniRule annotation1
Metal bindingi565ZincUniRule annotation1
Metal bindingi663ZincUniRule annotation1
Metal bindingi667ZincUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciCTRA272561:G1G18-800-MONOMER

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:CT_749
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000431 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000750881 – 875Alanine--tRNA ligaseAdd BLAST875

Structurei

3D structure databases

ProteinModelPortaliO84754
SMRiO84754
ModBaseiSearch...
MobiDBiSearch...

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.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CIM Bacteria
COG0013 LUCA
InParanoidiO84754
KOiK01872
OMAiFEMMAHH

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

Sequencei

Sequence statusi: Complete.

O84754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSNTLRSNF LKFYANRNHT PVASSPVFPH NDPSILFTNA GMNQFKNIFL
60 70 80 90 100
GKEQTSYTRA TTSQKCIRAG GKHNDLENVG HTSRHLTFFE MLGNFSFGDY
110 120 130 140 150
FKQDAISFAW EVSLSIFNFD PDFIYATVHE KDDEAFALWE KYLPTDRIFR
160 170 180 190 200
LTDKDNFWSM ADTGPCGFCS ELLFDRGEKF GKAASPLEDV DGERFLEYWN
210 220 230 240 250
LVFMEFNRTS DGTLLALQKK CVDTGAGLER LVSLLAETET VFEADVLRHL
260 270 280 290 300
ISKIENLSGT TYSPTEAKGA AFRVIADHIR SLSFAIADGL LPGNTERGYV
310 320 330 340 350
LRKILRRAVN YGKRLGFNRP FLADVVPSLV DVMGEAYPEL SASVTQIQEV
360 370 380 390 400
LTTEEEHFFK TLQRGGNLLQ QVLKSSASSA KISGEDAFKL KDTYGLPIDE
410 420 430 440 450
IALLAKDYNY AIDMDTFEKL EVEAKERSRK NTKKTKNDSD SVFQDLDPTN
460 470 480 490 500
TSEFIGYDTL SCDTFIEGII KYNEIASSLE EGDEGAIILR TTPFYAGKGG
510 520 530 540 550
QIGDSGEIFC ESGTFLVSHT IAPKAGLIVH LGKLSQGSLT TTMAVTAQVN
560 570 580 590 600
QNLRKKTANN HTGCHLLHKA LEMTLGEHIR QAGSYVDSQK IRLDFTHNKA
610 620 630 640 650
LSPEDLLAIE TLVNEKIREN DPVTIREVLY SDVMSSSEIK QFFGDKYGDI
660 670 680 690 700
VRVVSAGFSH ELCGGTHAQA TGDIGYFRIT KEHAVATGIR RIEATTGEDA
710 720 730 740 750
ENIAREQDVD LNEIATVIQS PKDQILVKIR SVMEEKKDLA KQVADLENQL
760 770 780 790 800
VQQQVKTLLT SCEKICDTSY LVYYLTEEEG QRIQHYANAI HKEIPTNFIS
810 820 830 840 850
LWITEKNGRY IVLSRVSDDL TKRGVQAHTL LAELLAPYGG RCGGKAISAQ
860 870
GSSAELPQIE FLNKTLRQWI STQLA
Length:875
Mass (Da):97,671
Last modified:May 30, 2000 - v2
Checksum:i81C2DA7B29A5D11D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA Translation: AAC68344.2
PIRiE71476
RefSeqiNP_220268.1, NC_000117.1
WP_010725333.1, NC_000117.1

Genome annotation databases

EnsemblBacteriaiAAC68344; AAC68344; CT_749
GeneIDi35551122
884543
KEGGictr:CT_749
PATRICifig|272561.5.peg.823

Similar proteinsi

Entry informationi

Entry nameiSYA_CHLTR
AccessioniPrimary (citable) accession number: O84754
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: March 28, 2018
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

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