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O28029

- SYA_ARCFU

UniProt

O28029 - SYA_ARCFU

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Protein
Alanine--tRNA ligase
Gene
alaS, AF_2255
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

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).UniRule annotation

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. ATP binding Source: UniProtKB-HAMAP
  2. alanine-tRNA ligase activity Source: UniProtKB-HAMAP
  3. aminoacyl-tRNA editing activity Source: UniProtKB
  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
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

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 UniRule annotation

GO - Cellular componenti

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

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 ligaseUniRule annotation
PRO_0000075260Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-48856N.
STRINGi224325.AF2255.

Structurei

Secondary structure

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.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 97 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

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