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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi562 – 5621ZincUniRule annotation
Metal bindingi566 – 5661ZincUniRule annotation
Metal bindingi664 – 6641ZincUniRule annotation
Metal bindingi668 – 6681ZincUniRule annotation

GO - Molecular functioni

  1. alanine-tRNA ligase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP
  3. tRNA binding Source: UniProtKB-KW
  4. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. alanyl-tRNA aminoacylation Source: UniProtKB-HAMAP
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

BioCyciBAPH198804:GHMG-408-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:BUsg_390
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 883883Alanine--tRNA ligasePRO_0000075080Add
BLAST

Proteomic databases

PRIDEiQ8K9E7.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi198804.BUsg390.

Structurei

3D structure databases

ProteinModelPortaliQ8K9E7.
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

eggNOGiCOG0013.
KOiK01872.
OMAiPCSEIHI.
OrthoDBiEOG6Q2SQ2.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. 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.
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.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K9E7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTTNEIRQ SFLNFFKEKE HVIVPSSSLI PENDSTLLFT NAGMNQFKEY
60 70 80 90 100
FLGQKKKFYP RVTTVQNCLR TGGKHNDLEN VGYTKRHHTF FEMLGNFSFN
110 120 130 140 150
DYFKKEAITY AWELLTSRKW FNIDKNKLWI SVYEDDEETY KIWRDIIRIP
160 170 180 190 200
CHHIVKIGSK NNSQYDSENF WQMGETGPCG PCTEIFYNYD DSNKSNDFLK
210 220 230 240 250
DKNESFIEIW NIVFIEFNRI SKTKIVPLIN KSIDTGMGLE RISAVLQNVH
260 270 280 290 300
SNYKIDIFQK LIQKISNFTE IKDLNNISLK IIADHIRSCA FLIAENILPS
310 320 330 340 350
NEHRGYVLRR IIRRALRHGH KIGIKNNFFY KLVPSLIEIM GDSAKILRKK
360 370 380 390 400
EKIIEETLKI EEIQFSQTLD KGLKILNAEI KKSTNKTISG KTAFYLYDTF
410 420 430 440 450
GFPIDLTSDI CSEKNIKIDF KGFNIAKEEQ KKRSSIKNKF YKDYNKDIII
460 470 480 490 500
NDTCIFEGYK KNKTKSLVKY IFIKNESVFL IYKGQTATIF LDKTSFYPES
510 520 530 540 550
GGQIGDIGEL YHKKSRFIVE NTKKYGDTIG HYGKLISGKI IVNDSIYSKI
560 570 580 590 600
NHVYRNAIQL NHSATHLLHA ALQKVLGKNA IQKGSLVSNT HLRFDFSYSG
610 620 630 640 650
NINLSQIQNI ENIINKKIRS NDLIKIKNLS LEEAKKKKAI ALFDYKYQSS
660 670 680 690 700
VRVVFIKDFS IELCGGTHTK RTGNIGLFKI IEQSSVSSGI KRIEAVTGQQ
710 720 730 740 750
AIDYLHIKDN DMQNISFLLK CQNSKITEKI KKIIIQVEKL EKKTDQLQKR
760 770 780 790 800
ENIYQIKKLS KKINNIKGIN LLINTFTNYD QKSMKMIIDQ LKKELKISII
810 820 830 840 850
IFINKNKNDF TVIIRVTKNL INYITALKII NIFIKKANGK GGGKKEIAEG
860 870 880
GGMNIKKLPM ILNYIKSWIT IQLENIKTKN FNN
Length:883
Mass (Da):102,345
Last modified:September 30, 2002 - v1
Checksum:i7D1DB0D46F640AF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67942.1.
RefSeqiNP_660731.1. NC_004061.1.
WP_011053909.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67942; AAM67942; BUsg_390.
GeneIDi1005767.
KEGGibas:BUsg390.
PATRICi21247596. VBIBucAph100086_0403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67942.1.
RefSeqiNP_660731.1. NC_004061.1.
WP_011053909.1. NC_004061.1.

3D structure databases

ProteinModelPortaliQ8K9E7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg390.

Proteomic databases

PRIDEiQ8K9E7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67942; AAM67942; BUsg_390.
GeneIDi1005767.
KEGGibas:BUsg390.
PATRICi21247596. VBIBucAph100086_0403.

Phylogenomic databases

eggNOGiCOG0013.
KOiK01872.
OMAiPCSEIHI.
OrthoDBiEOG6Q2SQ2.

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-408-MONOMER.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. 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.
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.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiSYA_BUCAP
AccessioniPrimary (citable) accession number: Q8K9E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2002
Last sequence update: September 30, 2002
Last modified: March 31, 2015
This is version 80 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

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.