SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8K9E7

- SYA_BUCAP

UniProt

Q8K9E7 - SYA_BUCAP

Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.
    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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    Q8K9E7-1 [UniParc]FASTAAdd to Basket

    « Hide

    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...
    MobiDBi 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: October 1, 2014
    This is version 75 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