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O28029

- SYA_ARCFU

UniProt

O28029 - SYA_ARCFU

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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

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

Zn2+1 PublicationNote: 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
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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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 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 – 75Combined sources
Helixi11 – 144Combined sources
Turni15 – 173Combined sources
Beta strandi19 – 213Combined sources
Beta strandi25 – 284Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 384Combined sources
Beta strandi42 – 454Combined sources
Beta strandi55 – 584Combined sources
Helixi62 – 7413Combined sources
Turni75 – 773Combined sources
Beta strandi92 – 965Combined sources
Helixi100 – 1045Combined sources
Turni105 – 1106Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi116 – 12712Combined sources
Helixi129 – 1346Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 15513Combined sources
Helixi163 – 17614Combined sources
Helixi181 – 1833Combined sources
Beta strandi185 – 1939Combined sources
Beta strandi196 – 20510Combined sources
Beta strandi208 – 22013Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi231 – 24616Combined sources
Helixi247 – 2559Combined sources
Helixi260 – 2645Combined sources
Helixi266 – 2749Combined sources
Beta strandi282 – 2843Combined sources
Helixi285 – 30117Combined sources
Helixi307 – 32014Combined sources
Helixi324 – 35229Combined sources
Helixi361 – 37919Combined sources
Helixi386 – 39712Combined sources
Helixi405 – 43733Combined sources
Helixi442 – 45211Combined sources
Helixi456 – 46510Combined sources
Helixi476 – 4827Combined sources
Turni508 – 5103Combined sources
Beta strandi516 – 52510Combined sources
Beta strandi528 – 5347Combined sources
Beta strandi548 – 5525Combined sources
Beta strandi555 – 5595Combined sources
Beta strandi561 – 5655Combined sources
Beta strandi568 – 5725Combined sources
Beta strandi583 – 5886Combined sources
Helixi590 – 61425Combined sources
Beta strandi620 – 6223Combined sources
Beta strandi631 – 6355Combined sources
Helixi642 – 65716Combined sources
Beta strandi661 – 6688Combined sources
Helixi669 – 6768Combined sources
Helixi678 – 6814Combined sources
Beta strandi688 – 6969Combined sources
Beta strandi699 – 7024Combined sources
Helixi711 – 7144Combined sources
Beta strandi717 – 72610Combined sources
Beta strandi729 – 7379Combined sources
Helixi738 – 7403Combined sources
Helixi742 – 75615Combined sources
Turni757 – 7593Combined sources
Helixi762 – 7643Combined sources
Helixi765 – 79935Combined sources
Beta strandi803 – 8075Combined sources
Beta strandi809 – 8146Combined sources
Helixi819 – 83113Combined sources
Beta strandi834 – 8418Combined sources
Beta strandi843 – 85614Combined sources
Helixi858 – 86912Combined sources
Beta strandi871 – 8755Combined sources
Beta strandi877 – 88610Combined sources
Helixi890 – 90415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTLDEEYLDI TFLTENGFVR KRCPKCGKHF WTADPEREIC GDPPCESYSF
60 70 80 90 100
IGNPVFKKPF ELDEMREYYL NFFERRGHGR IERYPVVARW RTDIYLTIAS
110 120 130 140 150
IADFQPFVTS GVAPPPANPL TISQPCIRLD DLDSVGRTGR HLTLFEMMAH
160 170 180 190 200
HAFNYPGKEI YWKNETVAYC TELLNELGVK KEDIVYKEEP WAGGGNAGPC
210 220 230 240 250
LEAIVGGLEV ATLVFMNLEE HPEGDIEIKG ARYRKMDNYI VDTGYGLERF
260 270 280 290 300
VWASKGTPTV YDAIFPEVVD TIIDNSNVSF NREDERVRRI VAESSKLAGI
310 320 330 340 350
MGELRGERLN QLRKSVADTV GVSVEELEGI VVPLEKVYSL ADHTRCILFM
360 370 380 390 400
LGDGLVPSNA GAGYLARLMI RRSLRLAEEL ELGLDLYDLV EMHKKILGFE
410 420 430 440 450
FDVPLSTVQE ILELEKERYR TTVSKGTRLV ERLVERKKKL EKDDLIELYD
460 470 480 490 500
SHGIPVELAV GIAAEKGAEV EMPKDIYAEL AKRHSKAEKV QEKKITLQNE
510 520 530 540 550
YPATEKLYYD DPTLLEFEAE VIGVEGDFVI LNRSAFYPES GGQDNDVGYL
560 570 580 590 600
IANGGKFEVV DVLEADGVVL HVVKGAKPEV GTKVKGVIDS DVRWRHMRHH
610 620 630 640 650
SATHVLLYSL QKVLGNHVWQ AGARKEFSKA RLDVTHFRRP SEEEIKEIEM
660 670 680 690 700
LANREILANK PIKWEWMDRI EAERKFGFRL YQGGVPPGRK IRVVQVGDDV
710 720 730 740 750
QACGGTHCRS TGEIGMLKIL KVESIQDGVI RFEFAAGEAA IEAVEEMERL
760 770 780 790 800
LREASSILRV EPAKLPKTVE RFFEEWKDQR KEIERLKSVI ADLWADILME
810 820 830 840 850
RAEEFDSMKV VAEVVDADMQ ALQKLAERLA EKGAVGCLMA KGEGKVFVVT
860 870 880 890 900
FSGQKYDARE LLREIGRVAK GSGGGRKDVA QGAVQQLLDR EEMLDVIFRF

LSEHEG
Length:906
Mass (Da):102,536
Last modified:January 1, 1998 - v1
Checksum:i2AD39B7B65C72C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89002.1.
PIRiG69531.
RefSeqiNP_071080.1. NC_000917.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89002.1 .
PIRi G69531.
RefSeqi NP_071080.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 100 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