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O28029

- SYA_ARCFU

UniProt

O28029 - SYA_ARCFU

Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi600 – 6001Zinc
    Metal bindingi604 – 6041Zinc
    Metal bindingi703 – 7031Zinc
    Metal bindingi707 – 7071Zinc

    GO - Molecular functioni

    1. alanine-tRNA ligase activity Source: UniProtKB-HAMAP
    2. aminoacyl-tRNA editing activity Source: UniProtKB
    3. ATP binding Source: UniProtKB-HAMAP
    4. metal ion binding Source: UniProtKB-KW
    5. tRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. alanyl-tRNA aminoacylation Source: UniProtKB
    2. regulation of translational fidelity Source: GOC

    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

    BioCyciAFUL224325:GJBC-2303-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:AF_2255
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    ProteomesiUP000002199: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi703 – 7031C → A: Loss of tRNA editing activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 906906Alanine--tRNA ligasePRO_0000075260Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-48856N.
    STRINGi224325.AF2255.

    Structurei

    Secondary structure

    1
    906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 75
    Helixi11 – 144
    Turni15 – 173
    Beta strandi19 – 213
    Beta strandi25 – 284
    Beta strandi30 – 323
    Beta strandi42 – 454
    Beta strandi55 – 584
    Helixi62 – 7413
    Turni75 – 773
    Beta strandi92 – 965
    Helixi100 – 1045
    Turni105 – 1106
    Beta strandi111 – 1133
    Beta strandi116 – 12712
    Helixi129 – 1346
    Turni135 – 1373
    Beta strandi138 – 1403
    Beta strandi143 – 15513
    Helixi163 – 17614
    Helixi181 – 1833
    Beta strandi185 – 1939
    Beta strandi196 – 20510
    Beta strandi208 – 22013
    Beta strandi226 – 2283
    Beta strandi231 – 24616
    Helixi247 – 2559
    Helixi260 – 2645
    Helixi266 – 2749
    Helixi285 – 30117
    Helixi307 – 32014
    Helixi324 – 35229
    Helixi361 – 37919
    Helixi386 – 39712
    Helixi405 – 43733
    Helixi442 – 45211
    Helixi456 – 46510
    Helixi476 – 4827
    Turni508 – 5103
    Beta strandi516 – 52510
    Beta strandi528 – 5347
    Beta strandi548 – 5525
    Beta strandi555 – 5595
    Beta strandi561 – 5655
    Beta strandi568 – 5725
    Beta strandi583 – 5886
    Helixi590 – 61425
    Beta strandi620 – 6223
    Beta strandi631 – 6355
    Helixi642 – 65716
    Beta strandi661 – 6688
    Helixi669 – 6768
    Helixi678 – 6814
    Beta strandi688 – 6969
    Beta strandi699 – 7024
    Helixi711 – 7144
    Beta strandi717 – 72610
    Beta strandi729 – 7379
    Helixi738 – 7403
    Helixi742 – 75615
    Turni757 – 7593
    Helixi765 – 79935
    Beta strandi803 – 8075
    Beta strandi809 – 8146
    Helixi819 – 83113
    Beta strandi834 – 8418
    Beta strandi843 – 85614
    Helixi858 – 86912
    Beta strandi877 – 88610
    Helixi890 – 90415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZTGX-ray2.20A1-739[»]
    2ZVFX-ray3.20A/B/C/D/E/F/G/H737-906[»]
    3WQYX-ray3.30A/B1-906[»]
    3WQZX-ray3.49A/B1-906[»]
    ProteinModelPortaliO28029.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO28029.

    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.1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0013.
    KOiK01872.
    OMAiKYHTATH.

    Family and domain databases

    HAMAPiMF_00036_A. Ala_tRNA_synth_A.
    InterProiIPR002318. Ala-tRNA-lgiase_IIc.
    IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
    IPR018165. Ala-tRNA-synth_IIc_core.
    IPR018164. Ala-tRNA-synth_IIc_N.
    IPR022429. Ala-tRNA_lgiase_arc.
    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.
    TIGRFAMsiTIGR03683. A-tRNA_syn_arch. 1 hit.
    TIGR00344. alaS. 1 hit.
    PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O28029-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLDEEYLDI TFLTENGFVR KRCPKCGKHF WTADPEREIC GDPPCESYSF    50
    IGNPVFKKPF ELDEMREYYL NFFERRGHGR IERYPVVARW RTDIYLTIAS 100
    IADFQPFVTS GVAPPPANPL TISQPCIRLD DLDSVGRTGR HLTLFEMMAH 150
    HAFNYPGKEI YWKNETVAYC TELLNELGVK KEDIVYKEEP WAGGGNAGPC 200
    LEAIVGGLEV ATLVFMNLEE HPEGDIEIKG ARYRKMDNYI VDTGYGLERF 250
    VWASKGTPTV YDAIFPEVVD TIIDNSNVSF NREDERVRRI VAESSKLAGI 300
    MGELRGERLN QLRKSVADTV GVSVEELEGI VVPLEKVYSL ADHTRCILFM 350
    LGDGLVPSNA GAGYLARLMI RRSLRLAEEL ELGLDLYDLV EMHKKILGFE 400
    FDVPLSTVQE ILELEKERYR TTVSKGTRLV ERLVERKKKL EKDDLIELYD 450
    SHGIPVELAV GIAAEKGAEV EMPKDIYAEL AKRHSKAEKV QEKKITLQNE 500
    YPATEKLYYD DPTLLEFEAE VIGVEGDFVI LNRSAFYPES GGQDNDVGYL 550
    IANGGKFEVV DVLEADGVVL HVVKGAKPEV GTKVKGVIDS DVRWRHMRHH 600
    SATHVLLYSL QKVLGNHVWQ AGARKEFSKA RLDVTHFRRP SEEEIKEIEM 650
    LANREILANK PIKWEWMDRI EAERKFGFRL YQGGVPPGRK IRVVQVGDDV 700
    QACGGTHCRS TGEIGMLKIL KVESIQDGVI RFEFAAGEAA IEAVEEMERL 750
    LREASSILRV EPAKLPKTVE RFFEEWKDQR KEIERLKSVI ADLWADILME 800
    RAEEFDSMKV VAEVVDADMQ ALQKLAERLA EKGAVGCLMA KGEGKVFVVT 850
    FSGQKYDARE LLREIGRVAK GSGGGRKDVA QGAVQQLLDR EEMLDVIFRF 900
    LSEHEG 906
    Length:906
    Mass (Da):102,536
    Last modified:January 1, 1998 - v1
    Checksum:i2AD39B7B65C72C8B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89002.1.
    PIRiG69531.
    RefSeqiNP_071080.1. NC_000917.1.
    WP_010879744.1. NC_000917.1.

    Genome annotation databases

    EnsemblBacteriaiAAB89002; AAB89002; AF_2255.
    GeneIDi1485486.
    KEGGiafu:AF2255.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89002.1 .
    PIRi G69531.
    RefSeqi NP_071080.1. NC_000917.1.
    WP_010879744.1. NC_000917.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZTG X-ray 2.20 A 1-739 [» ]
    2ZVF X-ray 3.20 A/B/C/D/E/F/G/H 737-906 [» ]
    3WQY X-ray 3.30 A/B 1-906 [» ]
    3WQZ X-ray 3.49 A/B 1-906 [» ]
    ProteinModelPortali O28029.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48856N.
    STRINGi 224325.AF2255.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB89002 ; AAB89002 ; AF_2255 .
    GeneIDi 1485486.
    KEGGi afu:AF2255.

    Phylogenomic databases

    eggNOGi COG0013.
    KOi K01872.
    OMAi KYHTATH.

    Enzyme and pathway databases

    BioCyci AFUL224325:GJBC-2303-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O28029.

    Family and domain databases

    HAMAPi MF_00036_A. Ala_tRNA_synth_A.
    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.
    IPR022429. Ala-tRNA_lgiase_arc.
    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 TIGR03683. A-tRNA_syn_arch. 1 hit.
    TIGR00344. alaS. 1 hit.
    PROSITEi PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
      Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
      , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
      Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
    2. "Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii."
      Fukunaga R., Yokoyama S.
      Acta Crystallogr. D 63:390-400(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-703.
    3. "Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization."
      Naganuma M., Sekine S., Fukunaga R., Yokoyama S.
      Proc. Natl. Acad. Sci. U.S.A. 106:8489-8494(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-739 WITH AN ALANYL-ADENYLATE ANALOG, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 737-906, FUNCTION, ZINC-BINDING, COFACTOR, SUBUNIT, DOMAIN.

    Entry informationi

    Entry nameiSYA_ARCFU
    AccessioniPrimary (citable) accession number: O28029
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 98 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3