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Q8K9E7

- SYA_BUCAP

UniProt

Q8K9E7 - SYA_BUCAP

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Protein
Alanine--tRNA ligase
Gene
alaS, BUsg_390
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi562 – 5621Zinc Reviewed prediction
Metal bindingi566 – 5661Zinc Reviewed prediction
Metal bindingi664 – 6641Zinc Reviewed prediction
Metal bindingi668 – 6681Zinc Reviewed prediction

GO - Molecular functioni

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

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 ligase (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Gene namesi
Name:alaS
Ordered Locus Names:BUsg_390
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 ligaseUniRule annotation
PRO_0000075080Add
BLAST

Proteomic databases

PRIDEiQ8K9E7.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi198804.BUsg390.

Structurei

3D structure databases

ProteinModelPortaliQ8K9E7.

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.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0013.
KOiK01872.
OMAiYDIDIFQ.
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

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MKKTTNEIRQ SFLNFFKEKE HVIVPSSSLI PENDSTLLFT NAGMNQFKEY    50
FLGQKKKFYP RVTTVQNCLR TGGKHNDLEN VGYTKRHHTF FEMLGNFSFN 100
DYFKKEAITY AWELLTSRKW FNIDKNKLWI SVYEDDEETY KIWRDIIRIP 150
CHHIVKIGSK NNSQYDSENF WQMGETGPCG PCTEIFYNYD DSNKSNDFLK 200
DKNESFIEIW NIVFIEFNRI SKTKIVPLIN KSIDTGMGLE RISAVLQNVH 250
SNYKIDIFQK LIQKISNFTE IKDLNNISLK IIADHIRSCA FLIAENILPS 300
NEHRGYVLRR IIRRALRHGH KIGIKNNFFY KLVPSLIEIM GDSAKILRKK 350
EKIIEETLKI EEIQFSQTLD KGLKILNAEI KKSTNKTISG KTAFYLYDTF 400
GFPIDLTSDI CSEKNIKIDF KGFNIAKEEQ KKRSSIKNKF YKDYNKDIII 450
NDTCIFEGYK KNKTKSLVKY IFIKNESVFL IYKGQTATIF LDKTSFYPES 500
GGQIGDIGEL YHKKSRFIVE NTKKYGDTIG HYGKLISGKI IVNDSIYSKI 550
NHVYRNAIQL NHSATHLLHA ALQKVLGKNA IQKGSLVSNT HLRFDFSYSG 600
NINLSQIQNI ENIINKKIRS NDLIKIKNLS LEEAKKKKAI ALFDYKYQSS 650
VRVVFIKDFS IELCGGTHTK RTGNIGLFKI IEQSSVSSGI KRIEAVTGQQ 700
AIDYLHIKDN DMQNISFLLK CQNSKITEKI KKIIIQVEKL EKKTDQLQKR 750
ENIYQIKKLS KKINNIKGIN LLINTFTNYD QKSMKMIIDQ LKKELKISII 800
IFINKNKNDF TVIIRVTKNL INYITALKII NIFIKKANGK GGGKKEIAEG 850
GGMNIKKLPM ILNYIKSWIT IQLENIKTKN FNN 883
Length:883
Mass (Da):102,345
Last modified:October 1, 2002 - v1
Checksum:i7D1DB0D46F640AF8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67942.1.
RefSeqiNP_660731.1. NC_004061.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67942.1 .
RefSeqi NP_660731.1. NC_004061.1.

3D structure databases

ProteinModelPortali Q8K9E7.
ModBasei Search...

Protein-protein interaction databases

STRINGi 198804.BUsg390.

Proteomic databases

PRIDEi Q8K9E7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM67942 ; AAM67942 ; BUsg_390 .
GeneIDi 1005767.
KEGGi bas:BUsg390.
PATRICi 21247596. VBIBucAph100086_0403.

Phylogenomic databases

eggNOGi COG0013.
KOi K01872.
OMAi YDIDIFQ.
OrthoDBi EOG6Q2SQ2.

Enzyme and pathway databases

BioCyci BAPH198804:GHMG-408-MONOMER.

Family and domain databases

HAMAPi MF_00036_B. Ala_tRNA_synth_B.
InterProi 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.
IPR012947. tRNA_SAD.
[Graphical view ]
Pfami PF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view ]
PRINTSi PR00980. TRNASYNTHALA.
SMARTi SM00863. tRNA_SAD. 1 hit.
[Graphical view ]
SUPFAMi SSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsi TIGR00344. alaS. 1 hit.
PROSITEi PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 8, 2002
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 74 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

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